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PDXP | pyridoxal (pyridoxine, vitamin B6) phosphatase; Protein serine phosphatase that dephosphorylates ’Ser-3’ in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5’-phosphate (PLP), pyridoxine 5’-phosphate (PMP) and pyridoxine 5’-phosphate (PNP), with [...] (296 aa) | |||
PNPO | pyridoxamine 5’-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5’- phosphate (PNP) or pyridoxamine 5’-phosphate (PMP) into pyridoxal 5’-phosphate (PLP) (261 aa) | |||
SMARCC1 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1; Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene. Belongs to the neur [...] (1105 aa) | |||
SMARCC2 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2; Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR) [...] (1214 aa) | |||
PDXK | pyridoxal (pyridoxine, vitamin B6) kinase; Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (312 aa) | |||
LPP | LIM domain containing preferred translocation partner in lipoma; May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the [...] (612 aa) | |||
PRMT3 | protein arginine methyltransferase 3; Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins (531 aa) | |||
UBC | ubiquitin C (685 aa) | |||
PRMT2 | protein arginine methyltransferase 2; Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1- dependent manner). May be involved in growth regulation (433 aa) | |||
PHOSPHO2 | phosphatase, orphan 2; Phosphatase that has high activity toward pyridoxal 5’- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate (241 aa) | |||
PRMT6 | protein arginine methyltransferase 6; Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 ’Arg-2’ to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on hi [...] (375 aa) | |||
AOX1 | aldehyde oxidase 1 (1338 aa) | |||
PRMT8 | protein arginine methyltransferase 8; Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (394 aa) | |||
ELAVL1 | ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R); Involved in 3’-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA and AUUUUUA motifs. Binds preferentially to the 5’-UUUU[AG]UUU-3’ motif in vitro (326 aa) | |||
PRMT1 | protein arginine methyltransferase 1 (371 aa) | |||
MYSM1 | Myb-like, SWIRM and MPN domains 1; Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation (828 aa) |